메뉴 건너뛰기




Volumn 6, Issue 12, 1997, Pages 2548-2560

Cross-strand side-chain interactions versus turn conformation in β- hairpins

Author keywords

NMR; Peptide design; Protein folding; Side chain interactions; hairpin conformation; sheet twist; turn

Indexed keywords

PEPTIDE;

EID: 0031454065     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061207     Document Type: Article
Times cited : (74)

References (59)
  • 2
    • 0029028490 scopus 로고
    • α-Helix formation by peptides of defined sequence
    • Baldwin RL. 1995. α-Helix formation by peptides of defined sequence. Biophys Chem 55:127-135.
    • (1995) Biophys Chem , vol.55 , pp. 127-135
    • Baldwin, R.L.1
  • 3
    • 0000349003 scopus 로고
    • NMR evidence of a short linear peptide that folds into a β-hairpin in aqueous solution
    • Blanco FJ, Jiménez MA, Herranz J, Rico M, Santoro J, Nieto JL. 1993. NMR evidence of a short linear peptide that folds into a β-hairpin in aqueous solution. J Am Chem Soc 115:5887-5888.
    • (1993) J Am Chem Soc , vol.115 , pp. 5887-5888
    • Blanco, F.J.1    Jiménez, M.A.2    Herranz, J.3    Rico, M.4    Santoro, J.5    Nieto, J.L.6
  • 4
    • 0028301327 scopus 로고
    • NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluorethanol induced native-like β-hairpin formation
    • Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL. 1994a. NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluorethanol induced native-like β-hairpin formation. Biochemistry 33:6004-6014.
    • (1994) Biochemistry , vol.33 , pp. 6004-6014
    • Blanco, F.J.1    Jiménez, M.A.2    Pineda, A.3    Rico, M.4    Santoro, J.5    Nieto, J.L.6
  • 5
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable β-hairpin in aqueous solution
    • Blanco FJ, Rivas G, Serrano L. 1994b. A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Nature Struct Biol 1:584-590.
    • (1994) Nature Struct Biol , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 6
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By AA, Stephens RL, Lee JM, Warren CD, Jeanloz RW. 1984. Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame. J Am Chem Soc 106:811-813.
    • (1984) J Am Chem Soc , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 7
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler L, Ernst RR. 1983. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J Magn Reson 53:521-528.
    • (1983) J Magn Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 8
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid residues measured in aqueous solution of linear tetrapeptides H-Gly-Gly-X-Ala-OH
    • 1H NMR parameters of the common amino acid residues measured in aqueous solution of linear tetrapeptides H-Gly-Gly-X-Ala-OH. Biopolymers 18:285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wuthrich, K.2
  • 9
    • 0028672867 scopus 로고
    • Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins
    • Case DA, Dyson HJ, Wright PE. 1994. Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins. Methods Enzymol 239:392-416.
    • (1994) Methods Enzymol , vol.239 , pp. 392-416
    • Case, D.A.1    Dyson, H.J.2    Wright, P.E.3
  • 10
    • 0027423053 scopus 로고
    • Identification, classification, and analysis of β-bulges in proteins
    • Chan AW, Hutchinson EG, Harris D, Thornton JH. 1993. Identification, classification, and analysis of β-bulges in proteins. Protein Sci 2:1574-1590.
    • (1993) Protein Sci , vol.2 , pp. 1574-1590
    • Chan, A.W.1    Hutchinson, E.G.2    Harris, D.3    Thornton, J.H.4
  • 11
    • 0022313052 scopus 로고
    • Folding of the twisted β-sheet in bovine pancreatic trypsin inhibitor
    • Chou KC, Némethy G,. Pottle MS, Scheraga HA. 1985. Folding of the twisted β-sheet in bovine pancreatic trypsin inhibitor. Biochemistry 24:7948-7953.
    • (1985) Biochemistry , vol.24 , pp. 7948-7953
    • Chou, K.C.1    Némethy, G.2    Pottle, M.S.3    Scheraga, H.A.4
  • 12
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • Chou PY, Fasman GD. 1974. Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins. Biochemistry 13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 13
    • 0025014627 scopus 로고
    • PyBOP®: A new peptide coupling reagent devoid of toxic by-product
    • Coste J, Le-Nguyen D, Castro B. 1990. PyBOP®: A new peptide coupling reagent devoid of toxic by-product. Tetrahedron Lett 31:205-208.
    • (1990) Tetrahedron Lett , vol.31 , pp. 205-208
    • Coste, J.1    Le-Nguyen, D.2    Castro, B.3
  • 14
    • 0027364930 scopus 로고
    • Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin
    • Cox JPL, Evans PA, Packman LC, Williams DH, Woolfson DN. 1993. Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin. J Mol Biol 234:483-492.
    • (1993) J Mol Biol , vol.234 , pp. 483-492
    • Cox, J.P.L.1    Evans, P.A.2    Packman, L.C.3    Williams, D.H.4    Woolfson, D.N.5
  • 15
    • 0028857729 scopus 로고
    • Interactions responsible for the pH dependence of the β-hairpin conformational population formed by a designed linear peptide
    • de Alba E, Blanco FJ, Jiménez MA, Rico M, Nieto JL. 1995. Interactions responsible for the pH dependence of the β-hairpin conformational population formed by a designed linear peptide. Eur J Biochem 233:283-292.
    • (1995) Eur J Biochem , vol.233 , pp. 283-292
    • De Alba, E.1    Blanco, F.J.2    Jiménez, M.A.3    Rico, M.4    Nieto, J.L.5
  • 16
    • 1842403587 scopus 로고    scopus 로고
    • Turn residue sequence determines β-hairpin conformation in designed peptides
    • de Alba E, Jiménez MA, Rico M. 1997. Turn residue sequence determines β-hairpin conformation in designed peptides. J Am Chem Soc 119:175-183.
    • (1997) J Am Chem Soc , vol.119 , pp. 175-183
    • De Alba, E.1    Jiménez, M.A.2    Rico, M.3
  • 17
    • 0030334822 scopus 로고    scopus 로고
    • 1H NMR conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution
    • 1H NMR conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution. Folding & Design 1:133-144.
    • (1996) Folding & Design , vol.1 , pp. 133-144
    • De Alba, E.1    Jiménez, M.A.2    Rico, M.3    Nieto, J.L.4
  • 18
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson HJ, Wright PE. 1991. Defining solution conformations of small linear peptides. Annu Rev Biophys Chem 20:519-538.
    • (1991) Annu Rev Biophys Chem , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 19
  • 20
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Günter P, Braun W, Wüthrich K. 1991. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol 217:517-530.
    • (1991) J Mol Biol , vol.217 , pp. 517-530
    • Günter, P.1    Braun, W.2    Wüthrich, K.3
  • 21
    • 0030992473 scopus 로고    scopus 로고
    • Insights on β-hairpin stability in aqueous solution from peptides with enforced type I′ and type II′ β-turns
    • Haque TS, Gellman SH. 1997. Insights on β-hairpin stability in aqueous solution from peptides with enforced type I′ and type II′ β-turns. J Am Chem Soc 119:3301-3302.
    • (1997) J Am Chem Soc , vol.119 , pp. 3301-3302
    • Haque, T.S.1    Gellman, S.H.2
  • 22
    • 0000291574 scopus 로고
    • "Mirror image" reverse turns promote β-hairpin formation
    • Haque TS, Little JC, Gellman SH. 1994. "Mirror image" reverse turns promote β-hairpin formation. J Am Chem Soc 116:4105-4106.
    • (1994) J Am Chem Soc , vol.116 , pp. 4105-4106
    • Haque, T.S.1    Little, J.C.2    Gellman, S.H.3
  • 23
    • 0029931671 scopus 로고    scopus 로고
    • Stereochemical requirements for β-hairpin formation: Model studies with four-residue peptides and depsipeptides
    • Haque TS, Little JC, Gellman SH. 1996. Stereochemical requirements for β-hairpin formation: Model studies with four-residue peptides and depsipeptides. J Am Chem Soc 118:6975-6985.
    • (1996) J Am Chem Soc , vol.118 , pp. 6975-6985
    • Haque, T.S.1    Little, J.C.2    Gellman, S.H.3
  • 24
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J, Meier BH, Bachmann P, Ernst RA. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy.J Chem Phys 71:4546-4553.
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.A.4
  • 25
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 26
    • 0027411181 scopus 로고
    • Thermodynamic β-sheet propensities measured using a zinc-finger host peptide
    • Kim CA, Berg JM. 1993. Thermodynamic β-sheet propensities measured using a zinc-finger host peptide. Nature 362:267-270.
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 27
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59:631-660.
    • (1990) Annu Rev Biochem , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 28
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A, Ernst RR, Wüthrich K. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem Biophys Res Commun 95:1-6.
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 29
    • 0028849336 scopus 로고
    • Peptidomimetic host that binds a peptide guest affording a β-sheet structure that subsequently self-assembles. A simple receptor mimic
    • LaBrenz SR, Kelly JW. 1995. Peptidomimetic host that binds a peptide guest affording a β-sheet structure that subsequently self-assembles. A simple receptor mimic. J Am Chem Soc 117:1655-1656.
    • (1995) J Am Chem Soc , vol.117 , pp. 1655-1656
    • LaBrenz, S.R.1    Kelly, J.W.2
  • 31
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding SE, Rowe AJ, Horton JC, eds. Cambridge: Royal Society of Chemistry
    • Laue TM, Shak BD, Ridgeway TM, Pelletier SL. 1992. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC, eds. Analytical ultracentrifugation in biochemistry and polymer science. Cambridge: Royal Society of Chemistry, pp 90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shak, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 32
    • 0027391780 scopus 로고
    • Capping interactions in isolated α-helices: Position-dependent substitution effects and structure of a serine-capped peptide helix
    • Lyu PC, Wemmer DE, Zhou HX, Pinker RJ, Kallenbach NR. 1993. Capping interactions in isolated α-helices: Position-dependent substitution effects and structure of a serine-capped peptide helix. Biochemistry 32:421-425.
    • (1993) Biochemistry , vol.32 , pp. 421-425
    • Lyu, P.C.1    Wemmer, D.E.2    Zhou, H.X.3    Pinker, R.J.4    Kallenbach, N.R.5
  • 33
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor DL Jr, Kim PS. 1994a. Measurement of the β-sheet-forming propensities of amino acids. Nature 367:660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor Jr., D.L.1    Kim, P.S.2
  • 34
    • 0027998757 scopus 로고
    • Context is a major determinant of β-sheet propensity
    • Minor DL Jr, Kim PS. 1994b. Context is a major determinant of β-sheet propensity. Nature 371:264-261.
    • (1994) Nature , vol.371 , pp. 264-1261
    • Minor Jr., D.L.1    Kim, P.S.2
  • 35
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Muñoz V, Serrano L. 1994a. Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct Biol 1:399-409.
    • (1994) Nature Struct Biol , vol.1 , pp. 399-409
    • Muñoz, V.1    Serrano, L.2
  • 36
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: Comparison with experimental scales
    • Muñoz V, Serrano L. 1994b. Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: Comparison with experimental scales. Proteins Struct Funct Genet 20:301-311.
    • (1994) Proteins Struct Funct Genet , vol.20 , pp. 301-311
    • Muñoz, V.1    Serrano, L.2
  • 37
    • 0030037714 scopus 로고    scopus 로고
    • A 2,3′-substituted biphenyl-based amino acid facilitates the formation of a monomeric β-hairpin-like structure in aqueous solution at elevated temperature
    • Nesloney CL, Kelly JW. 1996. A 2,3′-substituted biphenyl-based amino acid facilitates the formation of a monomeric β-hairpin-like structure in aqueous solution at elevated temperature. J Am Chem Soc 118:5836-5845.
    • (1996) J Am Chem Soc , vol.118 , pp. 5836-5845
    • Nesloney, C.L.1    Kelly, J.W.2
  • 38
    • 0029670181 scopus 로고    scopus 로고
    • An artificial β-sheet comprising a molecular scaffold, a β-strand mimic, and a peptide strand
    • Nowick JS, Holmes DL, Mackin G, Noronha G, Shaka AJ, Smith EM. 1996a. An artificial β-sheet comprising a molecular scaffold, a β-strand mimic, and a peptide strand. J Am Chem Soc 118:2764-2765.
    • (1996) J Am Chem Soc , vol.118 , pp. 2764-2765
    • Nowick, J.S.1    Holmes, D.L.2    Mackin, G.3    Noronha, G.4    Shaka, A.J.5    Smith, E.M.6
  • 39
    • 0029975981 scopus 로고    scopus 로고
    • Triurea derivatives of diethylenetriamine as potential templates for the formation of artificial β-sheets
    • Nowick JS, Mahrus S, Smith EM, Ziller JW. 1996b. Triurea derivatives of diethylenetriamine as potential templates for the formation of artificial β-sheets. J Am Chem Soc 118:1066-1072.
    • (1996) J Am Chem Soc , vol.118 , pp. 1066-1072
    • Nowick, J.S.1    Mahrus, S.2    Smith, E.M.3    Ziller, J.W.4
  • 40
    • 0029891313 scopus 로고    scopus 로고
    • De novo design and structural analysis of a model β-hairpin peptide system
    • Ramírez-Alvarado M, Blanco FJ, Serrano L. 1996. De novo design and structural analysis of a model β-hairpin peptide system. Nature Struct Biol 3:604-612.
    • (1996) Nature Struct Biol , vol.3 , pp. 604-612
    • Ramírez-Alvarado, M.1    Blanco, F.J.2    Serrano, L.3
  • 41
    • 45949117739 scopus 로고
    • Improved techniques for homonuclear rotating-frame and isotropic mixing experiments
    • Rance M. 1987. Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J Magn Reson 74:557-564.
    • (1987) J Magn Reson , vol.74 , pp. 557-564
    • Rance, M.1
  • 42
    • 0028865129 scopus 로고
    • A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin
    • Searle MS, Williams DH, Packman LC. 1995. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin. Nature Struct Biol 2:999-1006.
    • (1995) Nature Struct Biol , vol.2 , pp. 999-1006
    • Searle, M.S.1    Williams, D.H.2    Packman, L.C.3
  • 43
    • 0030002295 scopus 로고    scopus 로고
    • Native-like β-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues
    • Searle MS, Zerella R, Williams DH, Packman LC. 1996. Native-like β-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues. Protein Eng 9:559-565.
    • (1996) Protein Eng , vol.9 , pp. 559-565
    • Searle, M.S.1    Zerella, R.2    Williams, D.H.3    Packman, L.C.4
  • 45
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering
    • Sibanda BL, Blundell TL, Thomton JM. 1989. Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering. J Mol Biol 206:759-777.
    • (1989) J Mol Biol , vol.206 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thomton, J.M.3
  • 46
    • 0021844602 scopus 로고
    • β-Hairpin families in globular proteins
    • Sibanda BL, Thornton JM. 1985. β-Hairpin families in globular proteins. Nature 316:170-174.
    • (1985) Nature , vol.316 , pp. 170-174
    • Sibanda, B.L.1    Thornton, J.M.2
  • 47
    • 0026351935 scopus 로고
    • Conformation of β-hairpins in protein structures. Classification and diversity in homologous structures
    • Sibanda BL, Thornton JM. 1991. Conformation of β-hairpins in protein structures. Classification and diversity in homologous structures. Methods Enzymol 202:59-82.
    • (1991) Methods Enzymol , vol.202 , pp. 59-82
    • Sibanda, B.L.1    Thornton, J.M.2
  • 48
    • 0028792105 scopus 로고
    • Guidelines for protein design. The energetics of β-sheet side chain interactions
    • Smith CK, Regan L. 1995. Guidelines for protein design. The energetics of β-sheet side chain interactions. Science 270:980-982.
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 49
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of amino acids
    • Smith CK, Withka JM, Regan L. 1994. A thermodynamic scale for the β-sheet forming tendencies of amino acids. Biochemistry 33:5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 50
    • 0029147823 scopus 로고
    • Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures
    • Swindells MB, Mac-Arthur MW, Thornton JM. 1995. Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures. Nature Struct Biol 2:596-603.
    • (1995) Nature Struct Biol , vol.2 , pp. 596-603
    • Swindells, M.B.1    Mac-Arthur, M.W.2    Thornton, J.M.3
  • 51
    • 0025398721 scopus 로고
    • WHATIF: A molecular modelling and drug design program
    • Vriend G. 1990. WHATIF: A molecular modelling and drug design program. J Mol Graph 8:52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 53
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart DS, Sykes BD. 1994. Chemical shifts as a tool for structure determination. Methods Enzymol 239:363-392.
    • (1994) Methods Enzymol , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 55
    • 0029058159 scopus 로고
    • An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters MA, Curmi PM. 1995. An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins Struct Fund Genet 22:119-131.
    • (1995) Proteins Struct Fund Genet , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.2
  • 57
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich K, Billeter M, Braun W. 1984. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J Mol Biol 180:715-740.
    • (1984) J Mol Biol , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 58
    • 0028036221 scopus 로고
    • Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: Evidence for an N-terminal capping box
    • Zhou HX, Lyu P, Wemmer DE, Kallenbach NR. 1994. Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: Evidence for an N-terminal capping box. Proteins Struct Funct Genet 18:1-7.
    • (1994) Proteins Struct Funct Genet , vol.18 , pp. 1-7
    • Zhou, H.X.1    Lyu, P.2    Wemmer, D.E.3    Kallenbach, N.R.4
  • 59
    • 0027245441 scopus 로고
    • A single-stranded amphipathic alpha-helix in aqueous solution: Design, structural characterization, and its application for determining alpha-helical propensities of amino acids
    • Zhou NE, Kay CM, Sykes BD, Hodges RS. 1993. A single-stranded amphipathic alpha-helix in aqueous solution: Design, structural characterization, and its application for determining alpha-helical propensities of amino acids. Biochemistry 32:6190-6197.
    • (1993) Biochemistry , vol.32 , pp. 6190-6197
    • Zhou, N.E.1    Kay, C.M.2    Sykes, B.D.3    Hodges, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.